ABCC7 p.Thr1115Ala
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PMID: 23955087
[PubMed]
Wang W et al: "Relative contribution of different transmembrane segments to the CFTR chloride channel pore."
No.
Sentence
Comment
160
Conductance was also unaltered in T1115A.
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ABCC7 p.Thr1115Ala 23955087:160:34
status: NEW167 Block by intracellular Au(CN)2 - was also significantly weakened in S1118A, S1118T, and T1115A compared to wild type, especially at hyperpolarized membrane potentials (Fig. 6); however, no apparent "U"-shape to the fractional current-voltage relationship was observed (Fig. 6b).
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ABCC7 p.Thr1115Ala 23955087:167:88
status: NEW180 As proposed previously for TM6 residue T338 [42], the channel is shown as being in an "outward facing" configuration when closed (with T1115 and S1118 accessible from the outside), and switching to an "inward facing" configuration on opening (with T1115 and S1118 accessible from the inside) S1118A and T1115A, although this increase was much less than that observed in T338A (Fig. 7b).
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ABCC7 p.Thr1115Ala 23955087:180:305
status: NEW183 Acetate permeability was slightly increased in S1118A and T1115A, but not significantly changed in S1118Q or S1118V (Fig. 8b).
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ABCC7 p.Thr1115Ala 23955087:183:58
status: NEW207 The effects of the S1118A mutation on permeant anion (Au(CN)2 - ) binding (Fig. 6), permeability of the lyotropic SCN- anion (Fig. 7), and permeability of the organic acetate anion (Fig. 8) were qualitatively similar to, but generally smaller than, those of T338A, and in fact similar effects were seen in T1115A.
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ABCC7 p.Thr1115Ala 23955087:207:306
status: NEW208 Neither S1118A nor T1115A significantly altered single channel conductance, although introduction of larger amino acid side chains in S1118Q and S1118V led to very small decreases in conductance (Fig. 5).
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ABCC7 p.Thr1115Ala 23955087:208:19
status: NEW211 Reduction of side chain volume in S1118A and T1115A, like T338A, led to an increase in the relative permeability of the small organic anion acetate, consistent with an increase in the apparent diameter of the narrowest region of the pore [25, 26]; however, introduction of side chains with larger volume (S1118Q, S1118V) did not lead to a decrease in acetate permeability (Fig. 8).
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ABCC7 p.Thr1115Ala 23955087:211:45
status: NEW217 One possible reason contributing to the minor functional effects observed in these experiments is that S1118A (and T1115A) might be considered relatively conservative mutations leading to only small changes in amino acid side chain volume.
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ABCC7 p.Thr1115Ala 23955087:217:115
status: NEW